Muscle and neuronal nicotinic acetylcholine receptors: structure, function and pathogenicity

D Kalamida, K Poulas, V Avramopoulou… - The FEBS …, 2007 - Wiley Online Library
Nicotinic acetylcholine receptors (nAChRs) are integral membrane proteins and prototypic
members of the ligand‐gated ion‐channel superfamily, which has precursors in the …

Three-finger α-neurotoxins and the nicotinic acetylcholine receptor, forty years on

S Nirthanan, MCE Gwee - Journal of pharmacological sciences, 2004 - jstage.jst.go.jp
The discovery, about forty years ago, of a-bungarotoxin, a three-finger a-neurotoxin from
Bungarus multicinctus venom, enabled the isolation of the nicotinic acetylcholine receptor …

Snake three-finger α-neurotoxins and nicotinic acetylcholine receptors: Molecules, mechanisms and medicine

S Nirthanan - Biochemical pharmacology, 2020 - Elsevier
Snake venom three-finger α-neurotoxins (α-3FNTx) act on postsynaptic nicotinic
acetylcholine receptors (nAChRs) at the neuromuscular junction (NMJ) to produce skeletal …

End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease

SM Sine - Physiological reviews, 2012 - journals.physiology.org
The synapse is a localized neurohumoral contact between a neuron and an effector cell and
may be considered the quantum of fast intercellular communication. Analogously, the …

Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine …

PHN Celie, RV Klaassen… - Journal of Biological …, 2005 - ASBMB
The crystal structure of acetylcholine-binding protein (AChBP) from the mollusk Lymnaea
stagnalis is the established model for the ligand binding domains of the ligand-gated ion …

The binding site of acetylcholine receptor as visualized in the X-ray structure of a complex between α-bungarotoxin and a mimotope peptide

M Harel, R Kasher, A Nicolas, JM Guss, M Balass… - Neuron, 2001 - cell.com
We have determined the crystal structure at 1.8 Å resolution of a complex of α-bungarotoxin
with a high affinity 13-residue peptide that is homologous to the binding region of the α …

Vicinal disulfide turns

O Carugo, M Čemažar, S Zahariev, I Hudáky… - Protein …, 2003 - academic.oup.com
The formation of a disulfide bond between adjacent cysteine residues is accompanied by
the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed …

Complex between α-bungarotoxin and an α7 nicotinic receptor ligand-binding domain chimaera

S Huang, SX Li, N Bren, K Cheng, R Gomoto… - Biochemical …, 2013 - portlandpress.com
To identify high-affinity interactions between long-chain α-neurotoxins and nicotinic
receptors, we determined the crystal structure of the complex between α-btx (α …

Experimentally based model of a complex between a snake toxin and the α7 nicotinic receptor

C Fruchart-Gaillard, B Gilquin… - Proceedings of the …, 2002 - National Acad Sciences
To understand how snake neurotoxins interact with nicotinic acetylcholine receptors, we
have elaborated an experimentally based model of the α–cobratoxin–α7 receptor complex …

[HTML][HTML] α-Bungarotoxin binding to acetylcholine receptor membranes studied by low angle X-ray diffraction

HS Young, LG Herbette, V Skita - Biophysical journal, 2003 - cell.com
The nicotinic acetylcholine receptor (nAChR) carries two binding sites for snake venom
neurotoxins. α-Bungarotoxin from the Southeast Asian banded krait, Bungarus multicinctus …